7fe5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 7fe5 is ON HOLD  until Paper Publication
==AvmM Catalyzes Macrocyclization in Alchivemycin A Biosynthesis==
<StructureSection load='7fe5' size='340' side='right'caption='[[7fe5]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fe5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._NBRC_109436 Streptomyces sp. NBRC 109436]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FE5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7fe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fe5 OCA], [https://pdbe.org/7fe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fe5 RCSB], [https://www.ebi.ac.uk/pdbsum/7fe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fe5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8F7LEJ5_9ACTN A0A8F7LEJ5_9ACTN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Macrocyclization is an important process that affords morphed scaffold in biosynthesis of bioactive natural products. Nature has adapted diverse biosynthetic strategies to form macrocycles. In this work, we report the identification and characterization of a small enzyme AvmM that can catalyze the construction of a 16-membered macrocyclic ring in the biosynthesis of alchivemycin A (1). We show through in vivo gene deletion, in vitro biochemical assay and isotope labelling experiments that AvmM catalyzes tandem dehydration and Michael-type addition to generate the core scaffold of 1. Mechanistic studies by crystallography, DFT calculations and MD simulations of AvmM reveal that the reactions are achieved with assistance from the special tenuazonic acid like moiety of substrate. Our results thus uncover an uncharacterized macrocyclization strategy in natural product biosynthesis.


Authors: Zhang, B., Ge, H.M.
AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis.,Zhu HJ, Zhang B, Wei W, Liu SH, Xiang L, Zhu J, Jiao RH, Igarashi Y, Bashiri G, Liang Y, Tan RX, Ge HM Nat Commun. 2022 Aug 3;13(1):4499. doi: 10.1038/s41467-022-32088-4. PMID:35922406<ref>PMID:35922406</ref>


Description: AvmM Catalyzes Macrocyclization in Alchivemycin A Biosynthesis
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zhang, B]]
<div class="pdbe-citations 7fe5" style="background-color:#fffaf0;"></div>
[[Category: Ge, H.M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. NBRC 109436]]
[[Category: Ge HM]]
[[Category: Zhang B]]

Latest revision as of 20:14, 29 November 2023

AvmM Catalyzes Macrocyclization in Alchivemycin A BiosynthesisAvmM Catalyzes Macrocyclization in Alchivemycin A Biosynthesis

Structural highlights

7fe5 is a 3 chain structure with sequence from Streptomyces sp. NBRC 109436. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.09Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A8F7LEJ5_9ACTN

Publication Abstract from PubMed

Macrocyclization is an important process that affords morphed scaffold in biosynthesis of bioactive natural products. Nature has adapted diverse biosynthetic strategies to form macrocycles. In this work, we report the identification and characterization of a small enzyme AvmM that can catalyze the construction of a 16-membered macrocyclic ring in the biosynthesis of alchivemycin A (1). We show through in vivo gene deletion, in vitro biochemical assay and isotope labelling experiments that AvmM catalyzes tandem dehydration and Michael-type addition to generate the core scaffold of 1. Mechanistic studies by crystallography, DFT calculations and MD simulations of AvmM reveal that the reactions are achieved with assistance from the special tenuazonic acid like moiety of substrate. Our results thus uncover an uncharacterized macrocyclization strategy in natural product biosynthesis.

AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis.,Zhu HJ, Zhang B, Wei W, Liu SH, Xiang L, Zhu J, Jiao RH, Igarashi Y, Bashiri G, Liang Y, Tan RX, Ge HM Nat Commun. 2022 Aug 3;13(1):4499. doi: 10.1038/s41467-022-32088-4. PMID:35922406[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Zhu HJ, Zhang B, Wei W, Liu SH, Xiang L, Zhu J, Jiao RH, Igarashi Y, Bashiri G, Liang Y, Tan RX, Ge HM. AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis. Nat Commun. 2022 Aug 3;13(1):4499. doi: 10.1038/s41467-022-32088-4. PMID:35922406 doi:http://dx.doi.org/10.1038/s41467-022-32088-4

7fe5, resolution 2.09Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA